Analytical Data
-
基因名
phrB
- Application
-
别名
DNA photolyase Photoreactivating enzyme
-
种属
Escherichia coli
-
表达系统
E. coli
-
标签
N- His-SUMO & C- Myc
-
纯度
Greater than 90% as determined by SDS-PAGE.
-
蛋白编号
P00914
-
表达区间
1-472aa
-
分子量
73.7 kDa
-
内毒素
< 1.0 EU per μg protein as determined by the LAL method.
-
性状
Freeze-dried powder
-
缓冲液
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
-
复溶方法
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- 个性化定制
-
稳定性测试
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
-
保存条件 & 期限
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
-
运输条件
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
The study of the PhrB protein, a key component in the regulatory mechanisms of bacterial communication, has gained significant attention in recent years. PhrB, or pleiotropic regulatory protein B, is primarily known for its role in quorum sensing, a process by which bacteria coordinate their behavior based on population density. This protein is particularly important in the context of *Bacillus subtilis*, a model organism for studying bacterial physiology. Research has shown that PhrB influences biofilm formation, sporulation, and the production of various exoenzymes, thereby impacting the development and survival strategies of the bacterial community. Furthermore, understanding PhrB's structure and function can provide insights into its interaction with other regulatory proteins, enabling the design of novel antimicrobial strategies that target bacterial communication pathways. Recombinant DNA technology has facilitated the production of PhrB in heterologous systems, allowing for detailed biochemical and structural analyses. This research not only uncovers the intricate networks of bacterial signaling but also addresses broader implications for infectious disease management and biotechnology applications. As such, the characterization of PhrB and its associated pathways represents a frontier in microbiological research, with the potential to revolutionize our approach to bacterial infections and microbial ecology.












